13C-nuclear magnetic resonance studies of 85% 13C-enriched amino acids and small peptides

Fermandjian, Serge; Tran-Dinh, S.; Šavrda, J.; Sala, E.; Mermet-Bouvier, R.; Bricas, E.; Fromageot, P.

doi:10.1016/0304-4165(75)90261-5

Cited by 39 publications

(8 citation statements)

References 51 publications

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“…These assignments give values of G(cis-trans) of 2.3 ppm for Pro3 and 2.8 ppm and 2.3 ppm for the cis a and cis b resonances of proline 2 a t p H 6.2. Typical values of the shift difference G(cis-trans) for proline C-3 resonances include 2.05 ppm for Gly-Pro, 2.15 ppm for Ala-Pro, 2.48 ppm for Val-Pro (Thomas & Williams, 1972), 2.18 ppm for Gly-Pro-Gly (Fermandjian et al, 1975), 1.97 ppm (pH 9) and 2.25 pprn (pH 1.6) for thyrotropin-releasing hormone (Haar et al, 1975), 2.2 ppm for poly(Pro-Gly) and 2.6 ppm for poly(Gly-Gly-Pro-Gly) (Torchia & Lyerla, 1974). The observation of only two resonances corresponding to cis-and trans-Pro3 C-3 indicates that the Pro3 C-3 resonance is sensitive only to the isomerism about the Pro-Pro bond.…”

Section: Resultsmentioning

confidence: 99%

¹³C nuclear magnetic resonance study of the cis-trans isomerism in X-Pro-Pro tripeptides

London¹,

Matwiyoff²,

Stewart³

et al. 1978

Biochemistry

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13C nuclear magnetic resonance has been used to characterize quantitatively the cis-trans isomerism about both peptide bonds in the tripeptides Ser-Pro-Pro and Arg-Pro-Pro. Detailed pH titration data indicate that the configuration about both peptide bonds is closely linked to titration of the terminal carboxyl group and, to a lesser extent, to titration of the terminal amino group. The Pro2 C-3 resonance has been found particularly useful for interpretation due to its sensitivity to the isomerization about both peptide bonds. Analysis of the probabilities of the trans-trans, cic-cis, cis-trans, and trans-cis isomers in aqueous solution indicates a stability decrease in the order given. Similarities in the isomerization behavior of the two peptides indicate that side chain interactions involving the first residue have very little effect on the observed cis/trans ratios. The sensitivity of the cis/trans ratio to titration of the terminal amino group is most readily explained on the basis of an indirect effect on carbonyl-carbonyl repulsion.

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Section: Resultsmentioning

confidence: 99%

¹³C nuclear magnetic resonance study of the cis-trans isomerism in X-Pro-Pro tripeptides

London¹,

Matwiyoff²,

Stewart³

et al. 1978

Biochemistry

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“…Reson., 22, 23 (1976). (19) Under similar conditions but with power = 10 mW the ratio, to the 12C lines, of the normalized maximum peak heights are 13Cmeta ~6,13Conho ~6.7, 13Cq = 10.6, and the fine structure is still observed, while with power = 170 mW the ratios are 13Cmeta. not measurable; 13Cortho ~4; 13CQ ~15, and all lines are now broad singlets.…”

mentioning

confidence: 90%

Studies of the pH dependence of carbon-13 shifts and carbon-carbon coupling constants of [U-13C]aspartic and -glutamic acids

London¹,

Walker²,

Kollman³

et al. 1978

J. Am. Chem. Soc.

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“…Depending markedly on pH in terminal polypeptide residues and free amino acids, [22,23] the 1 J CαC coupling constant is largely pH independent in intrachain residues, averaging 52.8 ± 1.8 Hz. [42,43] The 109 values of 1 in flavodoxin average 52.4 ± 1.9 Hz, essentially uncorrelated with secondary structure or hydrogen-bonding patterns.…”

Section: Introductionmentioning

confidence: 99%

Variation in protein C^α‐related one‐bond J couplings

Schmidt¹,

Howard²,

Maestre-Martínez³

et al. 2008

Magnetic Reson in Chemistry

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Four types of polypeptide (1)J(C alpha X) couplings are examined, involving the main-chain carbon C(alpha) and either of four possible substituents. A total 3105 values of (1)J(C alpha H alpha), (1)J(C alpha C beta), (1)J(C alpha C'), and (1)J(C alpha N') were collected from six proteins, averaging 143.4 +/- 3.3, 34.9 +/- 2.5, 52.6 +/- 0.9, and 10.7 +/- 1.2 Hz, respectively. Analysis of variances (ANOVA) reveals a variety of factors impacting on (1)J and ranks their relative statistical significance and importance to biomolecular NMR structure refinement. Accordingly, the spread in the (1)J values is attributed, in equal proportions, to amino-acid specific substituent patterns and to polypeptide-chain geometry, specifically torsions phi, psi, and chi(1) circumjacent to C(alpha). The (1)J coupling constants correlate with protein secondary structure. For alpha-helical phi, psi combinations, (1)J(C alpha H alpha) is elevated by more than one standard deviation (147.8 Hz), while both (1)J(C alpha N') and (1)J(C alpha C beta) fall short of their grand means (9.5 and 33.7 Hz). Rare positive phi torsion angles in proteins exhibit concomitant small (1)J(C alpha H alpha) and (1)J(C alpha N') (138.4 and 9.6 Hz) and large (1)J(C alpha C beta) (39.9 Hz) values. The (1)J(C alpha N') coupling varies monotonously over the phi torsion range typical of beta-sheet secondary structure and is largest (13.3 Hz) for phi around -160 degrees. All four coupling types depend on psi and thus help determine a torsion that is notoriously difficult to assess by traditional approaches using (3)J. Influences on (1)J stemming from protein secondary structure and other factors, such as amino-acid composition, are largely independent.

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13C-nuclear magnetic resonance studies of 85% 13C-enriched amino acids and small peptides

Cited by 39 publications

References 51 publications

¹³C nuclear magnetic resonance study of the cis-trans isomerism in X-Pro-Pro tripeptides

¹³C nuclear magnetic resonance study of the cis-trans isomerism in X-Pro-Pro tripeptides

Studies of the pH dependence of carbon-13 shifts and carbon-carbon coupling constants of [U-13C]aspartic and -glutamic acids

Variation in protein C^α‐related one‐bond J couplings

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13C-nuclear magnetic resonance studies of 85% 13C-enriched amino acids and small peptides

Cited by 39 publications

References 51 publications

13C nuclear magnetic resonance study of the cis-trans isomerism in X-Pro-Pro tripeptides

13C nuclear magnetic resonance study of the cis-trans isomerism in X-Pro-Pro tripeptides

Studies of the pH dependence of carbon-13 shifts and carbon-carbon coupling constants of [U-13C]aspartic and -glutamic acids

Variation in protein Cα‐related one‐bond J couplings

Contact Info

Product

Resources

About

¹³C nuclear magnetic resonance study of the cis-trans isomerism in X-Pro-Pro tripeptides

¹³C nuclear magnetic resonance study of the cis-trans isomerism in X-Pro-Pro tripeptides

Variation in protein C^α‐related one‐bond J couplings